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3FE4

Crystal Structure of Human Carbonic Anhydrase vi

Functional Information from GO Data
ChainGOidnamespacecontents
A0001580biological_processdetection of chemical stimulus involved in sensory perception of bitter taste
A0004089molecular_functioncarbonate dehydratase activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0008270molecular_functionzinc ion binding
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
B0001580biological_processdetection of chemical stimulus involved in sensory perception of bitter taste
B0004089molecular_functioncarbonate dehydratase activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0008270molecular_functionzinc ion binding
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 901
ChainResidue
AHIS111
AHIS113
AHIS138
AHOH370
AHOH371
AHOH374

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 911
ChainResidue
AASP200
AGLN202
AASP203
BGLU173
BHOH393
AGLU72
ATHR73
ATYR176

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 902
ChainResidue
BHIS111
BHIS113
BHIS138
BHOH352
BHOH375
BHOH376

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 910
ChainResidue
AGLU173
BGLU72
BASP200
BGLN202
BASP203

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdgirHviEIHIV
ChainResidueDetails
ASER124-VAL140

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"4628675","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
AHIS85
ATHR220

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
BHIS85
BTHR220

245663

PDB entries from 2025-12-03

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